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In this investigation, a new toxin gene encoding the peptide ImKTx1 was isolated from the venom gland of the scorpion <jats:italic>Isometrus maculates<\/jats:italic> by constructing cDNA library method, and the recombinant ImKTx1 peptide was characterized physiologically. The mature peptide of ImKTx1 has 39 amino acid residues including six cross\u2010linked cysteines. The electrophysiological experiments showed that the recombinant ImKTx1 peptide had a pharmacological profile where it inhibited Kv1.3 channel currents with IC<jats:sub>50<\/jats:sub> of 1.70 n\u00b1 1.35 \u00b5M, whereas 10 \u00b5M rImKTx1 peptide inhibited about 40% Kv1.1 and 42% Kv1.2 channel currents, respectively. In addition, 10 \u00b5M rImKTx1 had no effect on the Nav1.2 and Nav1.4 channel currents. Multiple sequence alignments showed that ImKTx1 had no homologous toxin peptide, but it was similar with Ca<jats:sup>2+<\/jats:sup> channel toxins from scorpion and spider in the arrangement of cysteine residues. These results indicate that ImKTx1 is a new Kv1.3 channel blocker with a unique primary structure. Our results indicate the diversity of K<jats:sup>+<\/jats:sup> channel toxins from scorpion venoms and also provide a new molecular template targeting Kv1.3 channel. \u00a9 2011 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25:244\u2013251, 2011; View this article online at <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/wileyonlinelibrary.com\">wileyonlinelibrary.com<\/jats:ext-link>. 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